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Analysis of the AAA+ chaperone clpB gene and stress-response expression in the halophilic methanogenic archaeon Methanohalophilus portucalensis, by C.-J. Shih and M.-C. Lai

Microbiology vol. 153, part 8, pp. 2572 - 2583

Fig. S1. Sequence alignment and secondary structure elements of ClpB/Hsp101/Hsp104. The amino acid sequences aligned were Methanohalophilu portucalensis (MpClpB), Escherichia coli (EcClpB), Methanococcoides burtonii (MbATPase), Methanospirillum hungatei (MhATPase), Arabidobsis thaliana (AtHsp101), Methanothermobacter thermoautotrophicus (MtClpA/B), Thermus thermophilus (TtClpB) and Saccharomyces cerevisiae (ScHsp104). Numbers indicate positions in the amino-acid sequence. Secondary structure elements (based on TtClpB) are shown as helices (α helices) and arrows (β strand). Identical residues are shaded. The conserved nucleotide-binding domains (NBD1 and NBD2) and two repeated Clp amino-terminal domain motifs (ClpN) are in bold boxes and thin boxes, respectively. Conserved Walker motifs (Walker A and Walker B) are indicated as star symbols and the dashed line indicates the middle region which forms the coiled-coil structure. [PDF] (675 kb)

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